7zi7: Difference between revisions

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'''Unreleased structure'''


The entry 7zi7 is ON HOLD  until 2024-04-07
==Crystal structure of dCK C4S-S74E mutant in complex with UDP and the OR0345 inhibitor==
<StructureSection load='7zi7' size='340' side='right'caption='[[7zi7]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[7zi7]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7ZI7 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7ZI7 FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.8&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=JCM:4-(4-azanylpyrimidin-2-yl)-N-[2-methyl-5-[4-[2-(4-methylpiperazin-1-yl)ethyl]phenyl]phenyl]-N-propyl-1,3-thiazol-2-amine'>JCM</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=UDP:URIDINE-5-DIPHOSPHATE'>UDP</scene></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=7zi7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7zi7 OCA], [https://pdbe.org/7zi7 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7zi7 RCSB], [https://www.ebi.ac.uk/pdbsum/7zi7 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7zi7 ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/DCK_HUMAN DCK_HUMAN] Required for the phosphorylation of the deoxyribonucleosides deoxycytidine (dC), deoxyguanosine (dG) and deoxyadenosine (dA). Has broad substrate specificity, and does not display selectivity based on the chirality of the substrate. It is also an essential enzyme for the phosphorylation of numerous nucleoside analogs widely employed as antiviral and chemotherapeutic agents.<ref>PMID:18377927</ref> <ref>PMID:20614893</ref>


Authors:  
==See Also==
 
*[[Cytochrome P450 3D structures|Cytochrome P450 3D structures]]
Description:  
== References ==
[[Category: Unreleased Structures]]
<references/>
__TOC__
</StructureSection>
[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Ben-Yaala K]]
[[Category: Betzi S]]
[[Category: Morelli X]]
[[Category: Rebuffet E]]
[[Category: Saez-Ayala M]]

Latest revision as of 11:03, 7 February 2024

Crystal structure of dCK C4S-S74E mutant in complex with UDP and the OR0345 inhibitorCrystal structure of dCK C4S-S74E mutant in complex with UDP and the OR0345 inhibitor

Structural highlights

7zi7 is a 1 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 1.8Å
Ligands:, ,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

DCK_HUMAN Required for the phosphorylation of the deoxyribonucleosides deoxycytidine (dC), deoxyguanosine (dG) and deoxyadenosine (dA). Has broad substrate specificity, and does not display selectivity based on the chirality of the substrate. It is also an essential enzyme for the phosphorylation of numerous nucleoside analogs widely employed as antiviral and chemotherapeutic agents.[1] [2]

See Also

References

  1. ↑ Sabini E, Hazra S, Ort S, Konrad M, Lavie A. Structural basis for substrate promiscuity of dCK. J Mol Biol. 2008 May 2;378(3):607-21. Epub 2008 Mar 3. PMID:18377927 doi:http://dx.doi.org/10.1016/j.jmb.2008.02.061
  2. ↑ Hazra S, Ort S, Konrad M, Lavie A. Structural and kinetic characterization of human deoxycytidine kinase variants able to phosphorylate 5-substituted deoxycytidine and thymidine analogues . Biochemistry. 2010 Aug 10;49(31):6784-90. PMID:20614893 doi:10.1021/bi100839e

7zi7, resolution 1.80Å

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